P07358 (CO8B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement component C8 beta chain

Alternative name(s):
Complement component 8 subunit beta

Gene names

Name:

C8B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
Subunit structure	Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. Component of the membrane attack complex (MAC). MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9. Ref.8 Ref.12
Subcellular location	Secreted.
Post-translational modification	N-glycosylated; contains one or two bound glycans. Not O-glycosylated. Ref.1 Ref.9
Polymorphism	The sequence shown is that of allotype C8B B.
Involvement in disease	Complement component 8 deficiency, 2 (C8D2) [MIM:613789]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Sequence similarities	Belongs to the complement C6/C7/C8/C9 family. Contains 1 EGF-like domain. Contains 1 LDL-receptor class A domain. Contains 1 MACPF domain. Contains 2 TSP type-1 domains.

Ontologies

Keywords
Biological process	Complement alternate pathway Complement pathway Cytolysis Immunity Innate immunity
Cellular component	Membrane attack complex Secreted
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation Traceable author statement PubMed 8098723. Source: ProtInc complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara membrane Traceable author statement Ref.1. Source: ProtInc membrane attack complex Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Potential

Propeptide

33 – 54

22

PRO_0000023591

Chain

55 – 591

537

Complement component C8 beta chain

PRO_0000023592

Regions

Domain

64 – 117

54

TSP type-1 1

Domain

120 – 157

38

LDL-receptor class A

Domain

158 – 504

347

MACPF

Domain

505 – 535

31

EGF-like

Domain

545 – 591

47

TSP type-1 2

Amino acid modifications

Modified residue

418

1

Phosphothreonine Ref.12

Glycosylation

70

1

C-linked (Man) Ref.9

Glycosylation

73

1

C-linked (Man) Ref.9

Glycosylation

101

1

N-linked (GlcNAc...) Potential

Glycosylation

243

1

N-linked (GlcNAc...) Ref.10 Ref.11

Glycosylation

551

1

C-linked (Man) Ref.9

Glycosylation

554

1

C-linked (Man) Ref.9

Disulfide bond

65 ↔ 100

Ref.12

Disulfide bond

76 ↔ 110

Ref.12

Disulfide bond

79 ↔ 116

Ref.12

Disulfide bond

122 ↔ 133

Ref.12

Disulfide bond

127 ↔ 146

Ref.12

Disulfide bond

140 ↔ 155

Ref.12

Disulfide bond

378 ↔ 403

Ref.12

Disulfide bond

503 ↔ 550

Ref.12

Disulfide bond

505 ↔ 521

Ref.12

Disulfide bond

508 ↔ 523

Ref.12

Disulfide bond

525 ↔ 534

Ref.12

Disulfide bond

557 ↔ 590

Ref.12

Natural variations

Natural variant

108

1

E → K.
Corresponds to variant rs12067507 [ dbSNP | Ensembl ].

VAR_027649

Natural variant

117

1

R → G in allotype C8B A. Ref.4 Ref.13
Corresponds to variant rs1013579 [ dbSNP | Ensembl ].

VAR_012642

Natural variant

261

1

P → L.
Corresponds to variant rs12085435 [ dbSNP | Ensembl ].

VAR_027650

Secondary structure

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591

Helix Strand Turn

Details...

Turn

78 – 81

4

Beta strand

82 – 86

5

Beta strand

89 – 91

3

Beta strand

104 – 109

6

Beta strand

123 – 126

4

Turn

128 – 130

3

Helix

136 – 138

3

Beta strand

141 – 143

3

Beta strand

146 – 149

4

Helix

172 – 176

5

Beta strand

177 – 179

3

Turn

181 – 183

3

Beta strand

186 – 189

4

Beta strand

201 – 205

5

Beta strand

208 – 212

5

Beta strand

216 – 221

6

Beta strand

229 – 236

8

Helix

237 – 240

4

Turn

256 – 258

3

Turn

269 – 271

3

Beta strand

272 – 275

4

Helix

276 – 283

8

Beta strand

290 – 297

8

Beta strand

299 – 306

8

Beta strand

308 – 310

3

Helix

315 – 321

7

Helix

330 – 340

11

Beta strand

342 – 352

11

Beta strand

355 – 361

7

Helix

362 – 365

4

Turn

366 – 369

4

Helix

372 – 378

7

Turn

379 – 381

3

Turn

404 – 408

5

Helix

409 – 412

4

Turn

413 – 415

3

Beta strand

419 – 426

8

Helix

435 – 439

5

Beta strand

441 – 443

3

Helix

449 – 457

9

Beta strand

461 – 469

9

Helix

470 – 473

4

Turn

476 – 478

3

Helix

482 – 499

18

Helix

502 – 504

3

Beta strand

513 – 517

5

Beta strand

520 – 524

5

Helix

532 – 534

3

Beta strand

536 – 541

6

Beta strand

557 – 563

7

Beta strand

584 – 588

5

Sequences

	Sequence		Length	Mass (Da)
	P07358 [UniParc]. Last modified January 23, 2002. Version 3. Checksum: B01722A6F2E9AFCE	FASTA	591	67,047
	10 20 30 40 50 60 MKNSRTWAWR APVELFLLCA ALGCLSLPGS RGERPHSFGS NAVNKSFAKS RQMRSVDVTL 70 80 90 100 110 120 MPIDCELSSW SSWTTCDPCQ KKRYRYAYLL QPSQFHGEPC NFSDKEVEDC VTNRPCRSQV 130 140 150 160 170 180 RCEGFVCAQT GRCVNRRLLC NGDNDCGDQS DEANCRRIYK KCQHEMDQYW GIGSLASGIN 190 200 210 220 230 240 LFTNSFEGPV LDHRYYAGGC SPHYILNTRF RKPYNVESYT PQTQGKYEFI LKEYESYSDF 250 260 270 280 290 300 ERNVTEKMAS KSGFSFGFKI PGIFELGISS QSDRGKHYIR RTKRFSHTKS VFLHARSDLE 310 320 330 340 350 360 VAHYKLKPRS LMLHYEFLQR VKRLPLEYSY GEYRDLFRDF GTHYITEAVL GGIYEYTLVM 370 380 390 400 410 420 NKEAMERGDY TLNNVHACAK NDFKIGGAIE EVYVSLGVSV GKCRGILNEI KDRNKRDTMV 430 440 450 460 470 480 EDLVVLVRGG ASEHITTLAY QELPTADLMQ EWGDAVQYNP AIIKVKVEPL YELVTATDFA 490 500 510 520 530 540 YSSTVRQNMK QALEEFQKEV SSCHCAPCQG NGVPVLKGSR CDCICPVGSQ GLACEVSYRK 550 560 570 580 590 NTPIDGKWNC WSNWSSCSGR RKTRQRQCNN PPPQNGGSPC SGPASETLDC S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementary DNA and derived amino acid sequence of the beta subunit of human complement protein C8: identification of a close structural and ancestral relationship to the alpha subunit and C9." Howard O.M.Z., Rao A.G., Sodetz J.M. Biochemistry 26:3565-3570(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION. Tissue: Liver.
[2]	Sodetz J.M. Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-117.
[5]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Complementary DNA cloning of complement C8 beta and its sequence homology to C9." Haefliger J.-A., Tschopp J., Nardelli D., Wahli W., Kocher H.-P., Tosi M., Stanley K.K. Biochemistry 26:3551-3556(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-591, PROTEIN SEQUENCE OF 55-68. Tissue: Liver.
[8]	"The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure." Steckel E.W., York R.G., Monahan J.B., Sodetz J.M. J. Biol. Chem. 255:11997-12005(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, SUBUNIT.
[9]	"The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues." Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O. J. Biol. Chem. 274:32786-32794(1999) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT TRP-70; TRP-73; TRP-551 AND TRP-554.
[10]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement." Lovelace L.L., Cooper C.L., Sodetz J.M., Lebioda L. J. Biol. Chem. 286:17585-17592(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 55-591, PHOSPHORYLATION AT THR-418, SUBUNIT, DISULFIDE BONDS.
[13]	"Human complement component C8. Molecular basis of the beta-chain polymorphism." Dewald G., Hemmer S., Noethen M.M. FEBS Lett. 340:211-215(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-117, DEFINITION OF ALLOTYPES C8B A AND C8B B.
+	Additional computationally mapped references.

Web resources

C8Bbase

C8B mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16973 mRNA. Translation: AAA51862.1.
AK313382 mRNA. Translation: BAG36180.1.
AL121998 Genomic DNA. Translation: CAC18532.1.
CH471059 Genomic DNA. Translation: EAX06641.1.
BC130575 mRNA. Translation: AAI30576.1.
X04393 mRNA. Translation: CAA27981.1.

IPI

IPI00294395.

PIR

C8HUB. A43071.

RefSeq

NP_000057.1. NM_000066.2.

UniGene

Hs.391835.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OJY	X-ray	2.51	B	55-591	[»]

ProteinModelPortal

P07358.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000360281.

PTM databases

PhosphoSite

P07358.

Polymorphism databases

DMDM

20141201.

Proteomic databases

PaxDb

P07358.

PeptideAtlas

P07358.

PRIDE

P07358.

Protocols and materials databases

DNASU

732.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371237; ENSP00000360281; ENSG00000021852.

GeneID

732.

KEGG

hsa:732.

UCSC

uc001cyp.3. human.

Organism-specific databases

CTD

732.

GeneCards

GC01M057311.

HGNC

HGNC:1353. C8B.

HPA

HPA023694.

MIM

120960. gene.
613789. phenotype.

neXtProt

NX_P07358.

Orphanet

169150. Immunodeficiency due to a late component of complements deficiency.

PharmGKB

PA25952.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG146647.

HOGENOM

HOG000231146.

HOVERGEN

HBG106489.

InParanoid

P07358.

KO

K03998.

OrthoDB

EOG469QTG.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P07358.

Bgee

P07358.

CleanEx

HS_C8B.

Genevestigator

P07358.

GermOnline

ENSG00000021852. Homo sapiens.

Family and domain databases

InterPro

IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]

Pfam

PF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
[Graphical view]

PRINTS

PR00764. COMPLEMENTC9.

SMART

SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]

SUPFAM

SSF57424. LDL_rcpt_classA_cys-rich. 1 hit.
SSF82895. TSP1. 2 hits.

PROSITE

PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
PS50026. EGF_3. False negative.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07358.

GenomeRNAi

732.

NextBio

2980.

SOURCE

Search...

Entry information

Entry name

CO8B_HUMAN

Accession

Primary (citable) accession number: P07358
Secondary accession number(s): A1L4K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.